adenosine diphosphate has been researched along with 5,5'-bis(8-(phenylamino)-1-naphthalenesulfonate) in 3 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 3 (100.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Horowitz, PM; Ybarra, J | 1 |
| Eisenstein, E; Fisher, KE; White, ZW | 1 |
| Fink, AL; Palleros, DR; Shi, L | 1 |
3 other study(ies) available for adenosine diphosphate and 5,5'-bis(8-(phenylamino)-1-naphthalenesulfonate)
| Article | Year |
|---|---|
Inactive GroEL monomers can be isolated and reassembled to functional tetradecamers that contain few bound peptides.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Anilino Naphthalenesulfonates; Chaperonin 60; Chromatography, Ion Exchange; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Fluorescent Dyes; Kinetics; Macromolecular Substances; Protein Conformation; Protein Denaturation; Protein Folding; Spectrophotometry, Ultraviolet; Thiosulfate Sulfurtransferase; Urea | 1995 |
A monomeric variant of GroEL binds nucleotides but is inactive as a molecular chaperone.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Anilino Naphthalenesulfonates; Binding Sites; Chaperonin 60; Chaperonins; Circular Dichroism; Cloning, Molecular; Escherichia coli; Fluorescent Dyes; Genetic Variation; Kinetics; Molecular Weight; Mutagenesis, Site-Directed; Phosphopyruvate Hydratase; Protein Binding; Protein Conformation; Protein Denaturation; Protein Folding; Recombinant Proteins; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Thiosulfate Sulfurtransferase | 1995 |
Protein conformational changes induced by 1,1'-bis(4-anilino-5-naphthalenesulfonic acid): preferential binding to the molten globule of DnaK.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Anilino Naphthalenesulfonates; Binding Sites; Chromatography, High Pressure Liquid; Circular Dichroism; Energy Transfer; Escherichia coli Proteins; Fluorescent Dyes; Heat-Shock Proteins; HSP70 Heat-Shock Proteins; Kinetics; Protein Conformation; Protein Folding; Spectrometry, Fluorescence; Temperature | 1994 |